1ygy
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1ygy.gif|left|200px]] | [[Image:1ygy.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1ygy", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | + | {{STRUCTURE_1ygy| PDB=1ygy | SCENE= }} | |
- | | | + | |
- | | | + | |
- | }} | + | |
'''Crystal Structure of D-3-Phosphoglycerate dehydrogenase From Mycobacterium tuberculosis''' | '''Crystal Structure of D-3-Phosphoglycerate dehydrogenase From Mycobacterium tuberculosis''' | ||
Line 30: | Line 27: | ||
[[Category: Sacchettini, J C.]] | [[Category: Sacchettini, J C.]] | ||
[[Category: TBSGC, TB Structural Genomics Consortium.]] | [[Category: TBSGC, TB Structural Genomics Consortium.]] | ||
- | [[Category: | + | [[Category: Oxidoreductase]] |
- | [[Category: | + | [[Category: Phosphoglycerate dehydrogenase]] |
- | [[Category: | + | [[Category: Protein structure initiative]] |
- | [[Category: | + | [[Category: Psi]] |
- | [[Category: | + | [[Category: Serine biosynthesis]] |
- | [[Category: | + | [[Category: Structural genomic]] |
- | [[Category: | + | [[Category: Tb structural genomics consortium]] |
- | [[Category: | + | [[Category: Tbsgc]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:18:13 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 13:18, 3 May 2008
Crystal Structure of D-3-Phosphoglycerate dehydrogenase From Mycobacterium tuberculosis
Overview
Phosphoglycerate dehydrogenases exist in at least three different structural motifs. The first D-3-phosphoglycerate dehydrogenase structure to be determined was from Escherichia coli and is a tetramer composed of identical subunits that contain three discernable structural domains. The crystal structure of D-3-phosphoglycerate dehydrogenase from Mycobacterium tuberculosis has been determined at 2.3 A. This enzyme represents a second structural motif of the D-3-phosphoglycerate dehydrogenase family, one that contains an extended C-terminal region. This structure is also a tetramer of identical subunits, and the extended motif of 135 amino acids exists as a fourth structural domain. This intervening domain exerts quite a surprising characteristic to the structure by introducing significant asymmetry in the tetramer. The asymmetric unit is composed of two identical subunits that exist in two different conformations characterized by rotation of approximately 180 degrees around a hinge connecting two of the four domains. This asymmetric arrangement results in the formation of two different and distinct domain interfaces between identical domains in the asymmetric unit. As a result, the surface of the intervening domain that is exposed to solvent in one subunit is turned inward in the other subunit toward the center of the structure where it makes contact with other structural elements. Significant asymmetry is also seen at the subunit level where different conformations exist at the NAD-binding site and the putative serine-binding site in the two unique subunits.
About this Structure
1YGY is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits., Dey S, Grant GA, Sacchettini JC, J Biol Chem. 2005 Apr 15;280(15):14892-9. Epub 2005 Jan 24. PMID:15668249 Page seeded by OCA on Sat May 3 16:18:13 2008
Categories: Mycobacterium tuberculosis | Phosphoglycerate dehydrogenase | Single protein | Dey, S. | Grant, G A. | Sacchettini, J C. | TBSGC, TB Structural Genomics Consortium. | Oxidoreductase | Protein structure initiative | Psi | Serine biosynthesis | Structural genomic | Tb structural genomics consortium | Tbsgc